PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
22403396-7	2012	Here we show that although both RRM1 and RRM2 expression are markedly induced in mouse uterine stromal cells undergoing decidualization, only RRM2 is regulated by progesterone, a key regulator of decidualization.	Progesterone	163-175	ribonucleotide reductase M2	Mus musculus	142-146
28507282-7	2017	Pharmacological inhibition of mTORC1 with rapamycin, mTOR kinase with AZD8055 or protein kinase B with MK2206 resulted in decrease of RRM1 and RRM2 in Rh30 cells both in vitro and in mouse tumor xenografts.	(5-(2,4-bis((3S)-3-methylmorpholin-4-yl)pyrido(2,3-d)pyrimidin-7-yl)-2-methoxyphenyl)methanol	70-77	ribonucleotide reductase M2	Mus musculus	143-147
28507282-7	2017	Pharmacological inhibition of mTORC1 with rapamycin, mTOR kinase with AZD8055 or protein kinase B with MK2206 resulted in decrease of RRM1 and RRM2 in Rh30 cells both in vitro and in mouse tumor xenografts.	MK 2206	103-109	ribonucleotide reductase M2	Mus musculus	143-147
28507282-10	2017	In addition, TP53 mutant cancer cells had elevation of RRM1 and RRM2, which was reduced by rapamycin.	Sirolimus	91-100	ribonucleotide reductase M2	Mus musculus	64-68
22517893-6	2012	In the present study, we found for the first time that 5-azaC is a potent inhibitor of RRM2 in leukemia cell lines, in a mouse model, and in BM mononuclear cells from acute myeloid leukemia (AML) patients.	Azacitidine	55-61	ribonucleotide reductase M2	Mus musculus	87-91
28797284-12	2017	Immunohistochemistry results demonstrated a downregulation of p-ERK, E2F1, and RRM2 in mice receiving gambogic acid treatment and combination treatment.	gambogic acid	102-115	ribonucleotide reductase M2	Mus musculus	79-83
22403396-12	2012	Therefore, RRM2 may be an important effector of progesterone signaling to induce cell proliferation and decidualization in mouse uterus.	Progesterone	48-60	ribonucleotide reductase M2	Mus musculus	11-15
22174045-11	2012	Downregulation of proteins, such as MAPK, matrin-3 and ribonucleotide reductase, subunit RRM2, which are implicated in cell proliferation, was also observed in TBTO-treated cells.	bis(tri-n-butyltin)oxide	160-164	ribonucleotide reductase M2	Mus musculus	89-93
21946215-4	2011	Truncations were tested mainly within a second RNA recognition motif (RRM2) of TDP-43; when the truncation site was more C-terminal in an RRM2 domain, a TDP-43 CTF basically became less soluble and more phosphorylated in differentiated Neuro2a cells.	CHEMBL408967	160-163	ribonucleotide reductase M2	Mus musculus	70-74
21946215-4	2011	Truncations were tested mainly within a second RNA recognition motif (RRM2) of TDP-43; when the truncation site was more C-terminal in an RRM2 domain, a TDP-43 CTF basically became less soluble and more phosphorylated in differentiated Neuro2a cells.	CHEMBL408967	160-163	ribonucleotide reductase M2	Mus musculus	138-142
21946215-5	2011	We also found that cleavage at the third beta-strand in RRM2 leads to the formation of SDS-resistant soluble oligomers.	Sodium Dodecyl Sulfate	87-90	ribonucleotide reductase M2	Mus musculus	56-60
21275172-0	2010	[Effect of cinobufotalin on growth of xenograft of endometrial carcinoma cell line ishikawa in nude mouse and its impact on RRM2 expression].	cinobufotalin	11-24	ribonucleotide reductase M2	Mus musculus	124-128
21275172-1	2010	OBJECTIVE: To investigate the inhibitory effect of cinobufotalin (CBT) on the growth of xenograft endometrial carcinoma cell line ishikawa in nude mice, and its impact on the expression of ribonucleotide reductase subunit M2 (RRM2).	cinobufotalin	51-64	ribonucleotide reductase M2	Mus musculus	189-224
21275172-1	2010	OBJECTIVE: To investigate the inhibitory effect of cinobufotalin (CBT) on the growth of xenograft endometrial carcinoma cell line ishikawa in nude mice, and its impact on the expression of ribonucleotide reductase subunit M2 (RRM2).	cinobufotalin	51-64	ribonucleotide reductase M2	Mus musculus	226-230
21275172-1	2010	OBJECTIVE: To investigate the inhibitory effect of cinobufotalin (CBT) on the growth of xenograft endometrial carcinoma cell line ishikawa in nude mice, and its impact on the expression of ribonucleotide reductase subunit M2 (RRM2).	cinobufotalin	66-69	ribonucleotide reductase M2	Mus musculus	189-224
21275172-1	2010	OBJECTIVE: To investigate the inhibitory effect of cinobufotalin (CBT) on the growth of xenograft endometrial carcinoma cell line ishikawa in nude mice, and its impact on the expression of ribonucleotide reductase subunit M2 (RRM2).	cinobufotalin	66-69	ribonucleotide reductase M2	Mus musculus	226-230
20731881-3	2010	The serum ALT elevation, with a peak at 24 h after Gal-N+LPS intoxication, was markedly augmented by means of the R1-mAb and R2-mAb.	Galactosamine	51-56	ribonucleotide reductase M2	Mus musculus	125-131
20731881-6	2010	Our in-vitro study showed that R1-mAb and R2-mAb significantly worsened the Gal-N+LPS-induced cytotoxicity and apoptosis of SEC mediated by caspase-3, which were almost of similar magnitude to those in the in-vivo study.	Galactosamine	76-81	ribonucleotide reductase M2	Mus musculus	42-44
16054677-2	2005	In common with other class Ia RRs, the enzyme is composed of two subunits (mR1 and mR2), with mR1 containing both the active site and allosteric effector sites and mR2 containing a stable tyrosyl radical that is essential for enzymatic activity.	Tyrosyl radical	188-203	ribonucleotide reductase M2	Mus musculus	83-86
18500819-3	2008	The second RRM (RRM2) is necessary and sufficient for tight, sequence-specific binding to the uridine-rich sequences buried around the 5" splice sites.	Uridine	94-101	ribonucleotide reductase M2	Mus musculus	11-14
18500819-3	2008	The second RRM (RRM2) is necessary and sufficient for tight, sequence-specific binding to the uridine-rich sequences buried around the 5" splice sites.	Uridine	94-101	ribonucleotide reductase M2	Mus musculus	16-20
18500819-7	2008	Interestingly, this characteristic beta-loop structure is conserved among a number of RRMs, including the U2AF65 RRM2 and the Sex-lethal RRM1 and RRM2, which also bind to uridine-rich RNAs.	Uridine	171-178	ribonucleotide reductase M2	Mus musculus	113-117
17848680-1	2007	PURPOSE: To prospectively determine the cellular iron uptake by using R2 and R2* mapping with multiecho readout gradient-echo and spin-echo sequences.	Iron	49-53	ribonucleotide reductase M2	Mus musculus	70-79
17848680-9	2007	R2 and R2* values were linearly correlated with cellular iron load, number of iron-loaded cells, and content of freely dissolved iron (r(2) range, 0.92-0.99; P < .001).	Iron	57-61	ribonucleotide reductase M2	Mus musculus	0-9
17848680-9	2007	R2 and R2* values were linearly correlated with cellular iron load, number of iron-loaded cells, and content of freely dissolved iron (r(2) range, 0.92-0.99; P < .001).	Iron	78-82	ribonucleotide reductase M2	Mus musculus	0-9
17848680-9	2007	R2 and R2* values were linearly correlated with cellular iron load, number of iron-loaded cells, and content of freely dissolved iron (r(2) range, 0.92-0.99; P < .001).	Iron	78-82	ribonucleotide reductase M2	Mus musculus	0-9
17848680-13	2007	CONCLUSION: Quantitative R2 and R2* mapping enables noninvasive estimations of cellular iron load and number of iron-labeled cells.	Iron	88-92	ribonucleotide reductase M2	Mus musculus	25-34
17848680-13	2007	CONCLUSION: Quantitative R2 and R2* mapping enables noninvasive estimations of cellular iron load and number of iron-labeled cells.	Iron	112-116	ribonucleotide reductase M2	Mus musculus	25-34
18500819-7	2008	Interestingly, this characteristic beta-loop structure is conserved among a number of RRMs, including the U2AF65 RRM2 and the Sex-lethal RRM1 and RRM2, which also bind to uridine-rich RNAs.	Uridine	171-178	ribonucleotide reductase M2	Mus musculus	146-150
16054677-2	2005	In common with other class Ia RRs, the enzyme is composed of two subunits (mR1 and mR2), with mR1 containing both the active site and allosteric effector sites and mR2 containing a stable tyrosyl radical that is essential for enzymatic activity.	Tyrosyl radical	188-203	ribonucleotide reductase M2	Mus musculus	164-167
9613846-7	1998	The lack of enzymatic activity in the mR1-cR2 complex is attributed to perturbation or elimination of interactions linking the tyrosine radical/dinuclear iron center and the C-terminus within R2.	tyrosine radical	127-143	ribonucleotide reductase M2	Mus musculus	43-45
12578384-5	2003	Analysis of the a-site D57N variant of mR1, which differs from wild-type mR1 (wt-mR1) in that its RR activity is activated by both ATP and dATP, demonstrates that dATP activation of the D57N variant RR arises from a blockage in the formation of mR1(4b) from mR1(4a), and provides strong evidence that mR1(4a) forms active complexes with mR2(2).	2'-deoxyadenosine triphosphate	163-167	ribonucleotide reductase M2	Mus musculus	337-340
12426144-8	2002	Fragment R1-2 was 90% homologous to a fragment of the DRIP/TRAP-80 (vitamin D receptor interacting protein/thyroid hormone receptor-activating protein 80) genes and was expressed in nontransformed but not in nickel-transformed cell lines.	Nickel	208-214	ribonucleotide reductase M2	Mus musculus	9-13
11781084-2	2002	Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors.	N,N-di-n-propylserotonin	13-17	ribonucleotide reductase M2	Mus musculus	113-116
11781084-2	2002	Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors.	Free Radicals	88-100	ribonucleotide reductase M2	Mus musculus	113-116
11781084-2	2002	Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors.	[[(2R,3S,4R,5S)-3,4-dihydroxy-5-methyloxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate	147-170	ribonucleotide reductase M2	Mus musculus	113-116
11781084-4	2002	In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer.	Adenosine Triphosphate	115-118	ribonucleotide reductase M2	Mus musculus	102-104
11781084-4	2002	In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer.	Adenosine Triphosphate	115-118	ribonucleotide reductase M2	Mus musculus	319-321
11781084-4	2002	In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer.	2'-deoxyadenosine triphosphate	122-126	ribonucleotide reductase M2	Mus musculus	102-104
11781084-4	2002	In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer.	2'-deoxyadenosine triphosphate	122-126	ribonucleotide reductase M2	Mus musculus	319-321
11781084-4	2002	In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer.	Adenine	142-149	ribonucleotide reductase M2	Mus musculus	102-104
11781084-4	2002	In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer.	Adenine	142-149	ribonucleotide reductase M2	Mus musculus	319-321
11781084-4	2002	In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer.	Adenosine Triphosphate	123-126	ribonucleotide reductase M2	Mus musculus	102-104
11781084-4	2002	In this model, nucleotide binding to the specificity site (s-site) drives formation of an active R1(2)R2(2) dimer, ATP or dATP binding to the adenine-specific site (a-site) results in formation of an inactive tetramer, and ATP binding to the newly described hexamerization site (h-site) drives formation of active R1(6)R2(6) hexamer.	Adenosine Triphosphate	123-126	ribonucleotide reductase M2	Mus musculus	319-321
11781084-9	2002	Our results suggest that the R1(6)R2(6) heterohexamer is the major active form of the enzyme in mammalian cells, and that the ATP concentration is the primary modulator of enzyme activity, coupling the rate of DNA biosynthesis with the energetic state of the cell.	Adenosine Triphosphate	126-129	ribonucleotide reductase M2	Mus musculus	34-36
11141086-1	2001	Mammalian ribonucleotide reductase, a chemotherapeutic target, has two subunits, mR1 and mR2, and is inhibited by AcF(1)TLDADF(7), denoted P7.	tldadf	120-126	ribonucleotide reductase M2	Mus musculus	89-92
15586357-2	2005	The enzyme is composed of 2 subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which competes with mR2 for binding to mR1.	acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine	71-81	ribonucleotide reductase M2	Mus musculus	46-49
15586357-2	2005	The enzyme is composed of 2 subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which competes with mR2 for binding to mR1.	acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine	71-81	ribonucleotide reductase M2	Mus musculus	131-134
15586357-2	2005	The enzyme is composed of 2 subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which competes with mR2 for binding to mR1.	acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine	71-81	ribonucleotide reductase M2	Mus musculus	131-134
15454215-2	2004	The enzyme is composed of two subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which disrupts mRR quaternary structure by competing with mR2 for binding to mR1.	acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine	73-83	ribonucleotide reductase M2	Mus musculus	48-51
15454215-2	2004	The enzyme is composed of two subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which disrupts mRR quaternary structure by competing with mR2 for binding to mR1.	acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine	73-83	ribonucleotide reductase M2	Mus musculus	133-136
15454215-2	2004	The enzyme is composed of two subunits (mR1 and mR2) and is inhibited by Ac-FTLDADF (denoted P7), corresponding to the C-terminus of mR2, which disrupts mRR quaternary structure by competing with mR2 for binding to mR1.	acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine	73-83	ribonucleotide reductase M2	Mus musculus	133-136
12578384-1	2003	Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors.	N,N-di-n-propylserotonin	13-17	ribonucleotide reductase M2	Mus musculus	113-116
12578384-1	2003	Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors.	Free Radicals	88-100	ribonucleotide reductase M2	Mus musculus	113-116
12578384-1	2003	Reduction of NDPs by murine ribonucleotide reductase (mRR) requires catalytic (mR1) and free radical-containing (mR2) subunits and is regulated by nucleoside triphosphate allosteric effectors.	[[(2R,3S,4R,5S)-3,4-dihydroxy-5-methyloxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate	147-170	ribonucleotide reductase M2	Mus musculus	113-116
12130552-7	2002	In contrast, mutation of this tryptophan to alanine in mR2 decreased the rate of internalization and inhibited basal signaling activity.	Tryptophan	30-40	ribonucleotide reductase M2	Mus musculus	55-58
12130552-7	2002	In contrast, mutation of this tryptophan to alanine in mR2 decreased the rate of internalization and inhibited basal signaling activity.	Alanine	44-51	ribonucleotide reductase M2	Mus musculus	55-58
11015199-3	2000	Peptide 3 is a cyclic analogue of the N-acetylated form of the heptapeptide C-terminus of the mR2 subunit (Ac-FTLDADF), which is the link between the two subunits and previously shown to be the minimal sequence inhibitor mRR by competing with mR2 for binding to mR1.	acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine	107-117	ribonucleotide reductase M2	Mus musculus	94-97
11015199-3	2000	Peptide 3 is a cyclic analogue of the N-acetylated form of the heptapeptide C-terminus of the mR2 subunit (Ac-FTLDADF), which is the link between the two subunits and previously shown to be the minimal sequence inhibitor mRR by competing with mR2 for binding to mR1.	acetyl-phenylalanyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine	107-117	ribonucleotide reductase M2	Mus musculus	243-246
9613846-7	1998	The lack of enzymatic activity in the mR1-cR2 complex is attributed to perturbation or elimination of interactions linking the tyrosine radical/dinuclear iron center and the C-terminus within R2.	Iron	154-158	ribonucleotide reductase M2	Mus musculus	43-45
34279079-0	2021	Triapine Analogues and Their Copper(II) Complexes: Synthesis, Characterization, Solution Speciation, Redox Activity, Cytotoxicity, and mR2 RNR Inhibition.	3-aminopyridine-2-carboxaldehyde thiosemicarbazone	0-8	ribonucleotide reductase M2	Mus musculus	135-138
34233591-5	2021	In an in vivo study, we established a streptozotocin-induced pregestational diabetes mellitus (PGDM) mouse model and found the fetal cardiac wall thickness in different regions to be dramatically increased in the PGDM grouValidation of DEMs and DEGs in the fetal heart showed significantly upregulated expression of let-7e-5p, miR-139-5p and miR-195-5p and downregulated expression of SGOL1, RRM2, RGS5, CDK1 and CENPA.	Streptozocin	38-52	ribonucleotide reductase M2	Mus musculus	392-396
8783260-11	1996	In the molecular layer cells were found expressing N-methyl-D-aspartate R1-4 and N-methyl-D-aspartate R2B and cells in the granule layer were found to express N-methyl-D-aspartate R1-1, N-methyl-D-aspartate R1-3 and N-methyl-D-aspartate R1-4 and N-methyl-D-aspartate R2C only.	N-Methylaspartate	51-71	ribonucleotide reductase M2	Mus musculus	72-76
34279079-11	2021	HL1 and 1 in the presence of 1,4-dithiothreitol are as potent inhibitors of mR2 ribonucleotide reductase as triapine.	Dithiothreitol	29-47	ribonucleotide reductase M2	Mus musculus	76-79
34279079-11	2021	HL1 and 1 in the presence of 1,4-dithiothreitol are as potent inhibitors of mR2 ribonucleotide reductase as triapine.	3-aminopyridine-2-carboxaldehyde thiosemicarbazone	108-116	ribonucleotide reductase M2	Mus musculus	76-79
34234118-6	2021	Notably, knockdown of MYBL2 sensitized CRC cells to treatment with MK-1775, a clinical trial drug for inhibition of WEE1, which is involved in a degradation pathway of RRM2.	adavosertib	67-74	ribonucleotide reductase M2	Mus musculus	168-172
34207929-0	2021	Coumarin-Based Triapine Derivatives and Their Copper(II) Complexes: Synthesis, Cytotoxicity and mR2 RNR Inhibition Activity.	3-aminopyridine-2-carboxaldehyde thiosemicarbazone	15-23	ribonucleotide reductase M2	Mus musculus	96-99
34249439-6	2021	Pterostilbene, a natural plant component, potently inhibited in vitro RR enzyme activity with the IC50 of about 0.62 muM through interacting with RRM2 protein, which was much higher than current RRM2 inhibitory drugs.	pterostilbene	0-13	ribonucleotide reductase M2	Mus musculus	146-150
34249439-12	2021	This study demonstrates that pterostilbene is a novel potent RR inhibitor by targeting RRM2.	pterostilbene	29-42	ribonucleotide reductase M2	Mus musculus	87-91
34207929-5	2021	In addition, their ability to reduce the tyrosyl radical in mouse R2 protein of ribonucleotide reductase has been ascertained by EPR spectroscopy and the results were compared with those for triapine.	cyclo(tyrosyl-tyrosyl)	41-48	ribonucleotide reductase M2	Mus musculus	66-68
34207929-5	2021	In addition, their ability to reduce the tyrosyl radical in mouse R2 protein of ribonucleotide reductase has been ascertained by EPR spectroscopy and the results were compared with those for triapine.	3-aminopyridine-2-carboxaldehyde thiosemicarbazone	191-199	ribonucleotide reductase M2	Mus musculus	66-68
32763454-0	2020	Osalmid, a novel identified RRM2 inhibitor, enhances radiosensitivity of esophageal cancer.	osalmide	0-7	ribonucleotide reductase M2	Mus musculus	28-32
35204799-0	2022	RRM2 Alleviates Doxorubicin-Induced Cardiotoxicity through the AKT/mTOR Signaling Pathway.	Doxorubicin	16-27	ribonucleotide reductase M2	Mus musculus	0-4
35204799-4	2022	However, the specific function of RRM2 in DOX-induced cardiotoxicity is yet to be determined.	Doxorubicin	42-45	ribonucleotide reductase M2	Mus musculus	34-38
35204799-5	2022	This study aimed to elucidate the role and potential mechanism of RRM2 on DOX-induced cardiotoxicity by investigating neonatal primary cardiomyocytes and mice treated with DOX.	Doxorubicin	74-77	ribonucleotide reductase M2	Mus musculus	66-70
35204799-9	2022	RRM2 overexpression, on the contrary, alleviated DOX-induced cardiotoxicity in vivo and in vitro.	Doxorubicin	49-52	ribonucleotide reductase M2	Mus musculus	0-4
35204799-10	2022	Consistently, DIDOX, an inhibitor of RRM2, attenuated the protective effect of RRM2.	3,4-dihydroxybenzohydroxamic acid	14-19	ribonucleotide reductase M2	Mus musculus	37-41
35204799-10	2022	Consistently, DIDOX, an inhibitor of RRM2, attenuated the protective effect of RRM2.	3,4-dihydroxybenzohydroxamic acid	14-19	ribonucleotide reductase M2	Mus musculus	79-83
35204799-11	2022	Mechanistically, we found that AKT/mTOR inhibitors could reverse the function of RRM2 overexpression on DOX-induced autophagy and apoptosis, which means that RRM2 could have regulated DOX-induced cardiotoxicity through the AKT/mTOR signaling pathway.	Doxorubicin	104-107	ribonucleotide reductase M2	Mus musculus	81-85
35204799-11	2022	Mechanistically, we found that AKT/mTOR inhibitors could reverse the function of RRM2 overexpression on DOX-induced autophagy and apoptosis, which means that RRM2 could have regulated DOX-induced cardiotoxicity through the AKT/mTOR signaling pathway.	Doxorubicin	104-107	ribonucleotide reductase M2	Mus musculus	158-162
35204799-11	2022	Mechanistically, we found that AKT/mTOR inhibitors could reverse the function of RRM2 overexpression on DOX-induced autophagy and apoptosis, which means that RRM2 could have regulated DOX-induced cardiotoxicity through the AKT/mTOR signaling pathway.	Doxorubicin	184-187	ribonucleotide reductase M2	Mus musculus	81-85
35204799-11	2022	Mechanistically, we found that AKT/mTOR inhibitors could reverse the function of RRM2 overexpression on DOX-induced autophagy and apoptosis, which means that RRM2 could have regulated DOX-induced cardiotoxicity through the AKT/mTOR signaling pathway.	Doxorubicin	184-187	ribonucleotide reductase M2	Mus musculus	158-162
35204799-12	2022	In conclusion, our experiment established that RRM2 could be a potential treatment in reversing DOX-induced cardiac dysfunction.	Doxorubicin	96-99	ribonucleotide reductase M2	Mus musculus	47-51
33577819-6	2021	Zn2+ binding sites were predicted in the TDP-43"s N-terminal domain, in the linker region between RRM1 and RRM2 domain, within RRM2 domain and at the junction of the RRM2 and C-terminal domain (CTD), but none in the 311-360 region of CTD.	Zinc	0-4	ribonucleotide reductase M2	Mus musculus	107-111
33577819-6	2021	Zn2+ binding sites were predicted in the TDP-43"s N-terminal domain, in the linker region between RRM1 and RRM2 domain, within RRM2 domain and at the junction of the RRM2 and C-terminal domain (CTD), but none in the 311-360 region of CTD.	Zinc	0-4	ribonucleotide reductase M2	Mus musculus	127-131
33577819-6	2021	Zn2+ binding sites were predicted in the TDP-43"s N-terminal domain, in the linker region between RRM1 and RRM2 domain, within RRM2 domain and at the junction of the RRM2 and C-terminal domain (CTD), but none in the 311-360 region of CTD.	Zinc	0-4	ribonucleotide reductase M2	Mus musculus	127-131
33577819-7	2021	Furthermore, we found that Zn2+ promotes the in vitro thioflavin-T-positive aggregations of C-terminal fragments (CTFs) termed TDP-432C and TDP-432C-A315T that encompass the RRM2 and CTD domains.	Zinc	27-31	ribonucleotide reductase M2	Mus musculus	174-178
32763454-3	2020	Previous studies have reported that Osalmid could act as an RRM2 inhibitor.	osalmide	36-43	ribonucleotide reductase M2	Mus musculus	60-64
33023155-4	2020	In mouse cells, iron shortage decreased protein abundance for iron-binding nucleotide metabolism enzymes (prominently XDH and ferritin homolog RRM2).	Iron	16-20	ribonucleotide reductase M2	Mus musculus	143-147
33023155-4	2020	In mouse cells, iron shortage decreased protein abundance for iron-binding nucleotide metabolism enzymes (prominently XDH and ferritin homolog RRM2).	Iron	62-66	ribonucleotide reductase M2	Mus musculus	143-147
31468165-9	2019	A higher MCS was associated with concurrent use of glucocorticoids and a higher baseline MCS (mR2 21.7%, cR2 25.1%).	mcs	9-12	ribonucleotide reductase M2	Mus musculus	94-97
31468165-9	2019	A higher MCS was associated with concurrent use of glucocorticoids and a higher baseline MCS (mR2 21.7%, cR2 25.1%).	mcs	89-92	ribonucleotide reductase M2	Mus musculus	94-97